Structure analysis

Mechanism of Aurora-B activation by INCENP and inhibition by Hesperadin.

X-ray diffraction
1.8Å resolution
Source organism: Xenopus laevis
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 15690.99 Å2
Buried surface area: 3586.2 Å2
Dissociation area: 1,793.1 Å2
Dissociation energy (ΔGdiss): 19.48 kcal/mol
Dissociation entropy (TΔSdiss): 11.14 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-126740
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 16042.44 Å2
Buried surface area: 3432.18 Å2
Dissociation area: 1,716.09 Å2
Dissociation energy (ΔGdiss): 17.32 kcal/mol
Dissociation entropy (TΔSdiss): 11.01 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-126740

Macromolecules

Chains: A, B
Length: 284 amino acids
Theoretical weight: 33.54 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6DE08 (Residues: 78-361; Coverage: 79%)
Gene names: airk2-a, aurkb-a
Pfam: Protein kinase domain
InterPro:
CATH:

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Chains: C, D
Length: 43 amino acids
Theoretical weight: 4.98 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O13024 (Residues: 798-840; Coverage: 5%)
Gene name: incenp-a
Pfam: Inner centromere protein, ARK binding region
InterPro: Inner centromere protein, ARK-binding domain
CATH: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

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